![]() ER stress signalling through eIF2α and CHOP, but not IRE1α, attenuates adipogenesis in mice. This study identified the role of p38 MAPK-mediated CHOP phosphorylation in adipocyte differentiation. Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP kinase. Transdifferentiation mediated tumor suppression by the endoplasmic reticulum stress sensor IRE-1 in C. Xbp1-independent Ire1 signaling is required for photoreceptor differentiation and rhabdomere morphogenesis in Drosophila. The transcription factor XBP-1 is essential for the development and survival of dendritic cells. Endoplasmic reticulum stress regulator XBP-1 contributes to effector CD8 + T cell differentiation during acute infection. Paneth cells as a site of origin for intestinal inflammation. Dual and opposing roles of the unfolded protein response regulated by IRE1α and XBP1 in proinsulin processing and insulin secretion. XBP1 controls maturation of gastric zymogenic cells by induction of MIST1 and expansion of the rough endoplasmic reticulum. XBP1 controls diverse cell type- and condition-specific transcriptional regulatory networks. The IRE1α/XBP1s pathway is essential for the glucose response and protection of β cells. XBP-1 regulates signal transduction, transcription factors and bone marrow colonization in B cells. XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation. The unfolded protein response sensor IRE1α is required at 2 distinct steps in B cell lymphopoiesis. This study was the first to demonstrate that XBP1 is required for the differentiation of plasma cells. Plasma cell differentiation requires the transcription factor XBP-1. This study showed that the function of the ER is regulated by the MAPK Slt2, not UPR pathways, in cell mitosis in budding yeast. A surveillance pathway monitors the fitness of the endoplasmic reticulum to control its inheritance. Calcium trafficking integrates endoplasmic reticulum function with mitochondrial bioenergetics. CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Chop deletion reduces oxidative stress, improves β cell function, and promotes cell survival in multiple mouse models of diabetes. Song, B., Scheuner, D., Ron, D., Pennathur, S. Antioxidants reduce endoplasmic reticulum stress and improve protein secretion. CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. IRE1 signaling affects cell fate during the unfolded protein response. Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins. Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Ppp1r15 gene knockout reveals an essential role for translation initiation factor 2 alpha (eIF2α) dephosphorylation in mammalian development. This study identified that CHOP and ATF4 form heterodimers, which leads to increased protein synthesis, oxidative stress and cell death. ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death. Translational control of mGluR-dependent long-term depression and object-place learning by eIF2α.
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